ArticleProceedings of the National Academy of Sciences of the United States of America2012
RecQ helicase translocates along single-stranded DNA with a moderate processivity and tight mechanochemical coupling.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- A CRISPR array orchestrates virulence and host response inMicrobiology spectrum · 2026Article
- Continuous-time random walk model for the diffusive motion of helicases.QRB discovery · 2025Article
- The toposiomerase IIIalpha-RMI1-RMI2 complex orients human Bloom's syndrome helicase for efficient disruption of D-loops.Nature communications · 2022Article
- Evaluation and modulation of DNA lesion bypass in an SV40 large T antigen-based in vitro replication system.FEBS open bio · 2021Article
- Measurement of Nucleotide Hydrolysis Using Fluorescent Biosensors for Phosphate.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Processivity, Velocity, and Universal Characteristics of Nucleic Acid Unwinding by Helicases.Biophysical journal · 2019Article
- Homology sensing via non-linear amplification of sequence-dependent pausing by RecQ helicase.eLife · 2019Article
- Competing interaction partners modulate the activity of Sgs1 helicase during DNA end resection.The EMBO journal · 2019Article
- Single molecule kinetics uncover roles for E. coli RecQ DNA helicase domains and interaction with SSB.Nucleic acids research · 2018Article
- RecQ helicase triggers a binding mode change in the SSB-DNA complex to efficiently initiate DNA unwinding.Nucleic acids research · 2017Article
- Shuttling along DNA and directed processing of D-loops by RecQ helicase support quality control of homologous recombination.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Single molecule measurements of DNA helicase activity with magnetic tweezers and t-test based step-finding analysis.Methods (San Diego, Calif.) · 2016Article
- Direct Fluorescent Imaging of Translocation and Unwinding by Individual DNA Helicases.Methods in enzymology · 2016Article
- Single-molecule visualization of RecQ helicase reveals DNA melting, nucleation, and assembly are required for processive DNA unwinding.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The HRDC domain of E. coli RecQ helicase controls single-stranded DNA translocation and double-stranded DNA unwinding rates without affecting mechanoenzymatic coupling.Scientific reports · 2015Article
- Mechanism of RecQ helicase mechanoenzymatic coupling reveals that the DNA interactions of the ADP-bound enzyme control translocation run terminations.Nucleic acids research · 2015Article
- A nucleotide-dependent and HRDC domain-dependent structural transition in DNA-bound RecQ helicase.The Journal of biological chemistry · 2014Article
- DNA helicases involved in DNA repair and their roles in cancer.Nature reviews. Cancer · 2013Review
- Yeast Pif1 helicase exhibits a one-base-pair stepping mechanism for unwinding duplex DNA.The Journal of biological chemistry · 2013Article
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Maintenance of genome integrity is the major biological role of RecQ-family helicases via their participation in homologous recombination (HR)-mediated DNA repair processes. RecQ helicases exert their functions by using the free energy of ATP hydrolysis for mechanical movement along DNA tracks (translocation). In addition to the importance of translocation per se in recombination processes, knowledge of its mechanism is necessary for the understanding of more complex translocation-based activities, including nucleoprotein displacement, strand separation (unwinding), and branch migration. Here, we report the key properties of the ssDNA translocation mechanism of Escherichia coli RecQ helicase, the prototype of the RecQ family. We monitored the pre-steady-state kinetics of ATP hydrolysis by RecQ and the dissociation of the enzyme from ssDNA during single-round translocation. We also gained information on the translocation mechanism from the ssDNA length dependence of the steady-state ssDNA-activated ATPase activity. We show that RecQ occludes 18 ± 2 nt on ssDNA during translocation. The hydrolysis of ATP is noncooperative in the presence of ssDNA, indicating that RecQ active sites work independently during translocation. In the applied conditions, the enzyme hydrolyzes 35 ± 4 ATP molecules per second during ssDNA translocation. RecQ translocates at a moderate processivity, with a mean run length of 100-320 nt on ssDNA. The determined tight mechanochemical coupling of 1.1 ± 0.2 ATP consumed per nucleotide traveled indicates an inchworm-type mechanism.
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